Strong Solute-Solute Dispersive Interactions in a Protein-Ligand Complex

Richard Malham, Sarah Johnstone, Richard J. Bingham, Elizabeth Barratt, Simon E V Phillips, Charles A. Laughton, Steve W. Homans

Research output: Contribution to journalArticlepeer-review

70 Citations (Scopus)

Abstract

The contributions of solute-solute dispersion interactions to binding thermodynamics have generally been thought to be small, due to the surmised equality between solute-solvent dispersion interactions prior to the interaction versus solute-solute dispersion interactions following the interaction. The thermodynamics of binding of primary alcohols to the major urinary protein (MUP-I) indicate that this general assumption is not justified. The enthalpy of binding becomes more favorable with increasing chain length, whereas the entropy of binding becomes less favorable, both parameters showing a linear dependence. Despite the hydrophobicity of the interacting species, these data show that binding is not dominated by the classical hydrophobic effect, but can be attributed to favorable ligand-protein dispersion interactions.

Original languageEnglish
Pages (from-to)17061-17067
Number of pages7
JournalJournal of the American Chemical Society
Volume127
Issue number48
DOIs
Publication statusPublished - 7 Dec 2005
Externally publishedYes

Fingerprint

Dive into the research topics of 'Strong Solute-Solute Dispersive Interactions in a Protein-Ligand Complex'. Together they form a unique fingerprint.

Cite this